Laminin, gamma 2

LAMC2
Identifiers
Aliases	LAMC2 , B2T, BM600, CSF, EBR2, EBR2A, LAMB2T, LAMNB2, Laminin, gamma 2, laminin subunit gamma 2
External IDs	OMIM: 150292 MGI: 99913 HomoloGene: 4062 GeneCards: LAMC2
Gene location (Human)
Chr.	Chromosome 1 (human)
End	183,245,127 bp
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)
End	153,186,447 bp
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• heparin binding ; • extracellular matrix structural constituent ;
Cellular component	• laminin-2 complex ; • perinuclear region of cytoplasm ; • basement membrane ; • cell cortex ; • membrane ; • extracellular region ; • extracellular space ; • GO:0005578 extracellular matrix ; • collagen-containing extracellular matrix ;
Biological process	• hemidesmosome assembly ; • cell adhesion ; • extracellular matrix organization ; • epidermis development ; • positive regulation of cell migration ; • positive regulation of cell population proliferation ; • system development ; • basement membrane assembly ; • animal organ morphogenesis ; • tissue development ; • cell migration ; • substrate adhesion-dependent cell spreading ;
	Sources:Amigo / QuickGO
Orthologs
	3918
	16782
	ENSG00000058085
	ENSMUSG00000026479
	Q13753
	Q61092
	NM_018891 ; NM_005562
	NM_008485
	NP_005553 ; NP_061486
	n/a
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated September 08, 2021

Laminin subunit gamma-2 is a protein that in humans is encoded by the LAMC2 gene.^[5]^[6]

Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene.

Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the gamma chain isoform laminin, gamma 2. The gamma 2 chain, formerly thought to be a truncated version of beta chain (B2t), is highly homologous to the gamma 1 chain; however, it lacks domain VI, and domains V, IV and III are shorter. It is expressed in several fetal tissues but differently from gamma 1, and is specifically localized to epithelial cells in skin, lung and kidney. The gamma 2 chain together with alpha 3 and beta 3 chains constitute laminin 5 (earlier known as kalinin), which is an integral part of the anchoring filaments that connect epithelial cells to the underlying basement membrane. The epithelium-specific expression of the gamma 2 chain implied its role as an epithelium attachment molecule, and mutations in this gene have been associated with junctional epidermolysis bullosa, a skin disease.^[6]

Related Research Articles

Keratin 14 is a member of the type I keratin family of intermediate filament proteins. Keratin 14 was the first type I keratin sequence determined. Keratin 14 is also known as cytokeratin-14 (CK-14) or keratin-14 (KRT14). In humans it is encoded by the KRT14 gene.

Keratin 18 is a type I cytokeratin. It is, together with its filament partner keratin 8, perhaps the most commonly found products of the intermediate filament gene family. They are expressed in single layer epithelial tissues of the body. Mutations in this gene have been linked to cryptogenic cirrhosis. Two transcript variants encoding the same protein have been found for this gene.

Hemidesmosomes are very small stud-like structures found in keratinocytes of the epidermis of skin that attach to the extracellular matrix. They are similar in form to desmosomes when visualized by electron microscopy, however, desmosomes attach to adjacent cells. Hemidesmosomes are also comparable to focal adhesions, as they both attach cells to the extracellular matrix. Instead of desmogleins and desmocollins in the extracellular space, hemidesmosomes utilize integrins. Hemidesmosomes are found in epithelial cells connecting the basal epithelial cells to the lamina lucida, which is part of the basal lamina. Hemidesmosomes are also involved in signaling pathways, such as keratinocyte migration or carcinoma cell intrusion.

The basement membrane is a thin, pliable sheet-like type of extracellular matrix, that provides cell and tissue support and acts as a platform for complex signalling. The basement membrane sits between epithelial tissues including mesothelium and endothelium, and the underlying connective tissue.

Laminin Protein in the extracellular matrix

Laminins are high-molecular weight proteins of the extracellular matrix. They are a major component of the basal lamina, a protein network foundation for most cells and organs. The laminins are an important and biologically active part of the basal lamina, influencing cell differentiation, migration, and adhesion.

Keratin 5, also known as KRT5, K5, or CK5, is a protein that is encoded in humans by the KRT5 gene. It dimerizes with keratin 14 and forms the intermediate filaments (IF) that make up the cytoskeleton of basal epithelial cells. This protein is involved in several diseases including epidermolysis bullosa simplex and breast and lung cancers.

Collagen XVII, previously called BP180, is a transmembrane protein which plays a critical role in maintaining the linkage between the intracellular and the extracellular structural elements involved in epidermal adhesion, identified by Diaz and colleagues in 1990.

Collagen alpha-1(VII) chain is a protein that in humans is encoded by the COL7A1 gene.

Integrin, beta 4 (ITGB4) also known as CD104, is a human gene.

Laminin subunit alpha-3 is a protein that in humans is encoded by the LAMA3 gene.

Laminin subunit beta-3 is a protein that in humans is encoded by the LAMB3 gene.

Laminin subunit alpha-1 is a protein that in humans is encoded by the LAMA1 gene.

Laminin subunit gamma-1 is a protein that in humans is encoded by the LAMC1 gene.

Laminin subunit beta-1 is a protein that in humans is encoded by the LAMB1 gene.

Laminin subunit alpha-2 is a protein that in humans is encoded by the LAMA2 gene.

Alpha-7 integrin is a protein that in humans is encoded by the ITGA7 gene. Alpha-7 integrin is critical for modulating cell-matrix interactions. Alpha-7 integrin is highly expressed in cardiac muscle, skeletal muscle and smooth muscle cells, and localizes to Z-disc and costamere structures. Mutations in ITGA7 have been associated with congenital myopathies and noncompaction cardiomyopathy, and altered expression levels of alpha-7 integrin have been identified in various forms of muscular dystrophy.

Laminin subunit alpha-4 is a protein that in humans is encoded by the LAMA4 gene.

Laminin subunit beta-2 is a protein that in humans is encoded by the LAMB2 gene.

Laminin subunit gamma-3 also known as LAMC3 is a protein that in humans is encoded by the LAMC3 gene.

Junctional epidermolysis bullosa is a skin condition characterized by blister formation within the lamina lucida of the basement membrane zone.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000058085 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000026479 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Kallunki P, Sainio K, Eddy R, Byers M, Kallunki T, Sariola H, Beck K, Hirvonen H, Shows TB, Tryggvason K (Nov 1992). "A truncated laminin chain homologous to the B2 chain: structure, spatial expression, and chromosomal assignment". J Cell Biol. 119 (3): 679–93. doi:10.1083/jcb.119.3.679. PMC 2289671 . PMID 1383240.
1 2 "Entrez Gene: LAMC2 laminin, gamma 2".

Baudoin C, Miquel C, Gagnoux-Palacios L, et al. (1995). "A novel homozygous nonsense mutation in the LAMC2 gene in patients with the Herlitz junctional epidermolysis bullosa". Hum. Mol. Genet. 3 (10): 1909–10. doi:10.1093/hmg/3.10.1909. PMID 7849725.
Burgeson RE, Chiquet M, Deutzmann R, et al. (1994). "A new nomenclature for the laminins". Matrix Biol. 14 (3): 209–11. doi:10.1016/0945-053X(94)90184-8. PMID 7921537.
Gedde-Dahl T, Dupuy BM, Jonassen R, et al. (1995). "Junctional epidermolysis bullosa inversa (locus EBR2A) assigned to 1q31 by linkage and association to LAMC1". Hum. Mol. Genet. 3 (8): 1387–91. doi:10.1093/hmg/3.8.1387. PMID 7987320.
Pulkkinen L, Christiano AM, Airenne T, et al. (1994). "Mutations in the gamma 2 chain gene (LAMC2) of kalinin/laminin 5 in the junctional forms of epidermolysis bullosa". Nat. Genet. 6 (3): 293–7. doi:10.1038/ng0394-293. PMID 8012393. S2CID 9915709.
Aberdam D, Galliano MF, Vailly J, et al. (1994). "Herlitz's junctional epidermolysis bullosa is linked to mutations in the gene (LAMC2) for the gamma 2 subunit of nicein/kalinin (LAMININ-5)". Nat. Genet. 6 (3): 299–304. doi:10.1038/ng0394-299. PMID 8012394. S2CID 2931644.
Miyazaki K, Kikkawa Y, Nakamura A, et al. (1994). "A large cell-adhesive scatter factor secreted by human gastric carcinoma cells". Proc. Natl. Acad. Sci. U.S.A. 90 (24): 11767–71. doi: 10.1073/pnas.90.24.11767 . PMC 48065 . PMID 8265624.
Vailly J, Verrando P, Champliaud MF, et al. (1994). "The 100-kDa chain of nicein/kalinin is a laminin B2 chain variant". Eur. J. Biochem. 219 (1–2): 209–18. doi: 10.1111/j.1432-1033.1994.tb19932.x . PMID 8306988.
Airenne T, Haakana H, Sainio K, et al. (1996). "Structure of the human laminin gamma 2 chain gene (LAMC2): alternative splicing with different tissue distribution of two transcripts". Genomics. 32 (1): 54–64. doi:10.1006/geno.1996.0076. PMID 8786121.
Mizushima H, Miyagi Y, Kikkawa Y, et al. (1997). "Differential expression of laminin-5/ladsin subunits in human tissues and cancer cell lines and their induction by tumor promoter and growth factors". J. Biochem. 120 (6): 1196–202. doi:10.1093/oxfordjournals.jbchem.a021541. PMID 9010770.
Mizushima H, Koshikawa N, Moriyama K, et al. (1998). "Wide distribution of laminin-5 gamma 2 chain in basement membranes of various human tissues". Horm. Res. 50 Suppl 2 (2): 7–14. doi:10.1159/000053118. PMID 9721586. S2CID 72456840.
Chen M, Marinkovich MP, Jones JC, et al. (1999). "NC1 domain of type VII collagen binds to the beta3 chain of laminin 5 via a unique subdomain within the fibronectin-like repeats". J. Invest. Dermatol. 112 (2): 177–83. doi: 10.1046/j.1523-1747.1999.00491.x . PMID 9989793.
Miller KA, Chung J, Lo D, et al. (2000). "Inhibition of laminin-5 production in breast epithelial cells by overexpression of p300". J. Biol. Chem. 275 (11): 8176–82. doi: 10.1074/jbc.275.11.8176 . PMID 10713141.
Olsen J, Lefebvre O, Fritsch C, et al. (2001). "Involvement of activator protein 1 complexes in the epithelium-specific activation of the laminin gamma2-chain gene promoter by hepatocyte growth factor (scatter factor)". Biochem. J. 347 (Pt 2): 407–17. doi:10.1042/0264-6021:3470407. PMC 1220973 . PMID 10749670.
Hirosaki T, Mizushima H, Tsubota Y, et al. (2000). "Structural requirement of carboxyl-terminal globular domains of laminin alpha 3 chain for promotion of rapid cell adhesion and migration by laminin-5". J. Biol. Chem. 275 (29): 22495–502. doi: 10.1074/jbc.M001326200 . PMID 10801807.
Amano S, Scott IC, Takahara K, et al. (2000). "Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 gamma 2 chain". J. Biol. Chem. 275 (30): 22728–35. doi: 10.1074/jbc.M002345200 . PMID 10806203.
Takizawa Y, Pulkkinen L, Chao SC, et al. (2000). "Mutation report: complete paternal uniparental isodisomy of chromosome 1: a novel mechanism for Herlitz junctional epidermolysis bullosa". J. Invest. Dermatol. 115 (2): 307–11. doi: 10.1046/j.1523-1747.2000.00052.x . PMID 10951251.
Manda R, Kohno T, Niki T, et al. (2000). "Differential expression of the LAMB3 and LAMC2 genes between small cell and non-small cell lung carcinomas". Biochem. Biophys. Res. Commun. 275 (2): 440–5. doi:10.1006/bbrc.2000.3331. PMID 10964684.
Spirito F, Chavanas S, Prost-Squarcioni C, et al. (2001). "Reduced expression of the epithelial adhesion ligand laminin 5 in the skin causes intradermal tissue separation". J. Biol. Chem. 276 (22): 18828–35. doi: 10.1074/jbc.M100381200 . PMID 11279058.
McArthur CP, Wang Y, Heruth D, Gustafson S (2001). "Amplification of extracellular matrix and oncogenes in tat-transfected human salivary gland cell lines with expression of laminin, fibronectin, collagens I, III, IV, c-myc and p53". Arch. Oral Biol. 46 (6): 545–55. doi:10.1016/S0003-9969(01)00014-0. PMID 11311202.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000058085 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000026479 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid1383240-5] Kallunki P, Sainio K, Eddy R, Byers M, Kallunki T, Sariola H, Beck K, Hirvonen H, Shows TB, Tryggvason K (Nov 1992). "A truncated laminin chain homologous to the B2 chain: structure, spatial expression, and chromosomal assignment". J Cell Biol. 119 (3): 679–93. doi:10.1083/jcb.119.3.679. PMC 2289671 . PMID 1383240.

[entrez-6] 1 2 "Entrez Gene: LAMC2 laminin, gamma 2".

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Laminin, gamma 2

Related Research Articles

References

Further reading